par Vassart, Gilbert 
;Refetoff, Samuel ;Brocas, Huguette;Dinsart, Christiane ;Dumont, Jacques
Référence Proceedings of the National Academy of Sciences of the United States of America, 72, 10, page (3839-3843)
Publication Publié, 1975-10
;Refetoff, Samuel ;Brocas, Huguette;Dinsart, Christiane ;Dumont, Jacques Référence Proceedings of the National Academy of Sciences of the United States of America, 72, 10, page (3839-3843)
Publication Publié, 1975-10
Article révisé par les pairs
| Résumé : | Thyroglobulin is a 19S protein of approximately 660,000 daltons and unknown quaternary structure. We have previously shown that a 33S mRNA purified from mammalian thyroids promoted synthesis in the Xenopus oocyte of a peptide immunologically related to thyroglobulin. Chemical identity to the native protein is now presented by means of a tryptic peptide analysis. Moreover, the 33S mRNA is shown to contain all the information required for the synthesis of a complete 19S thyroglobulin molecule. Gel filtration in Sepharose under denaturing conditions indicates that the reduced polypeptide encoded by the 33S mRNA is larger than 210,000 daltons. A model of a dimeric thyroglobulin with about 300,000 dalton subunits is presented. |
